Glutaconyl-CoA decarboxylase

In enzymology, a glutaconyl-CoA decarboxylase is an enzyme that catalyzes the chemical reaction


 * (2E)-glutaconyl-CoA + H+ + Na+ (in) $$\rightleftharpoons$$ (2E)-butenoyl-CoA + + Na+ (out)

Hence, this enzyme has one substrate, (2E)-glutaconyl-CoA, and two products, (2E)-butenoyl-CoA and CO2. During the process, an sodium ion is transported across the membrane. Previously, this enzyme was classified as EC 4.1.1.70.

This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is 4-carboxybut-2-enoyl-CoA carboxy-lyase (but-2-enoyl-CoA-forming). Other names in common use include glutaconyl coenzyme A decarboxylase, pent-2-enoyl-CoA carboxy-lyase, and 4-carboxybut-2-enoyl-CoA carboxy-lyase. This enzyme participates in benzoate degradation via coa ligation and butanoate metabolism.

As a decarboxylase, the enzyme requires biotin for its function.

Structural studies
As of mid-2024, five structures have been solved for this class of enzymes, with the PDB accession codes, , , and.